Phosphoproteomics in cancer

H. C. Harsha, Akhilesh Pandey

Research output: Contribution to journalReview article

99 Citations (Scopus)

Abstract

Reversible protein phosphorylation serves as a basis for regulating a number of cellular processes. Aberrant activation of kinase signaling pathways is commonly associated with several cancers. Recent developments in phosphoprotein/phosphopeptide enrichment strategies and quantitative mass spectrometry have resulted in robust pipelines for high-throughput characterization of phosphorylation in a global fashion. Today, it is possible to profile site-specific phosphorylation events on thousands of proteins in a single experiment. The potential of this approach is already being realized to characterize signaling pathways that govern oncogenesis. In addition, chemical proteomic strategies have been used to unravel targets of kinase inhibitors, which are otherwise difficult to characterize. This review summarizes various approaches used for analysis of the phosphoproteome in general, and protein kinases in particular, highlighting key cancer phosphoproteomic studies.

Original languageEnglish (US)
Pages (from-to)482-495
Number of pages14
JournalMolecular Oncology
Volume4
Issue number6
DOIs
StatePublished - Jan 1 2010
Externally publishedYes

Fingerprint

Phosphorylation
Phosphotransferases
Phosphopeptides
Neoplasms
Phosphoproteins
Proteomics
Protein Kinases
Mass Spectrometry
Carcinogenesis
Proteins

Keywords

  • Phosphorylation
  • Protein microarrays
  • Signal transduction
  • SILAC

ASJC Scopus subject areas

  • Molecular Medicine
  • Genetics
  • Cancer Research

Cite this

Phosphoproteomics in cancer. / Harsha, H. C.; Pandey, Akhilesh.

In: Molecular Oncology, Vol. 4, No. 6, 01.01.2010, p. 482-495.

Research output: Contribution to journalReview article

Harsha, H. C. ; Pandey, Akhilesh. / Phosphoproteomics in cancer. In: Molecular Oncology. 2010 ; Vol. 4, No. 6. pp. 482-495.
@article{281e62da7cf54a8e83fad85af9d5ce3e,
title = "Phosphoproteomics in cancer",
abstract = "Reversible protein phosphorylation serves as a basis for regulating a number of cellular processes. Aberrant activation of kinase signaling pathways is commonly associated with several cancers. Recent developments in phosphoprotein/phosphopeptide enrichment strategies and quantitative mass spectrometry have resulted in robust pipelines for high-throughput characterization of phosphorylation in a global fashion. Today, it is possible to profile site-specific phosphorylation events on thousands of proteins in a single experiment. The potential of this approach is already being realized to characterize signaling pathways that govern oncogenesis. In addition, chemical proteomic strategies have been used to unravel targets of kinase inhibitors, which are otherwise difficult to characterize. This review summarizes various approaches used for analysis of the phosphoproteome in general, and protein kinases in particular, highlighting key cancer phosphoproteomic studies.",
keywords = "Phosphorylation, Protein microarrays, Signal transduction, SILAC",
author = "Harsha, {H. C.} and Akhilesh Pandey",
year = "2010",
month = "1",
day = "1",
doi = "10.1016/j.molonc.2010.09.004",
language = "English (US)",
volume = "4",
pages = "482--495",
journal = "Molecular Oncology",
issn = "1574-7891",
publisher = "Elsevier",
number = "6",

}

TY - JOUR

T1 - Phosphoproteomics in cancer

AU - Harsha, H. C.

AU - Pandey, Akhilesh

PY - 2010/1/1

Y1 - 2010/1/1

N2 - Reversible protein phosphorylation serves as a basis for regulating a number of cellular processes. Aberrant activation of kinase signaling pathways is commonly associated with several cancers. Recent developments in phosphoprotein/phosphopeptide enrichment strategies and quantitative mass spectrometry have resulted in robust pipelines for high-throughput characterization of phosphorylation in a global fashion. Today, it is possible to profile site-specific phosphorylation events on thousands of proteins in a single experiment. The potential of this approach is already being realized to characterize signaling pathways that govern oncogenesis. In addition, chemical proteomic strategies have been used to unravel targets of kinase inhibitors, which are otherwise difficult to characterize. This review summarizes various approaches used for analysis of the phosphoproteome in general, and protein kinases in particular, highlighting key cancer phosphoproteomic studies.

AB - Reversible protein phosphorylation serves as a basis for regulating a number of cellular processes. Aberrant activation of kinase signaling pathways is commonly associated with several cancers. Recent developments in phosphoprotein/phosphopeptide enrichment strategies and quantitative mass spectrometry have resulted in robust pipelines for high-throughput characterization of phosphorylation in a global fashion. Today, it is possible to profile site-specific phosphorylation events on thousands of proteins in a single experiment. The potential of this approach is already being realized to characterize signaling pathways that govern oncogenesis. In addition, chemical proteomic strategies have been used to unravel targets of kinase inhibitors, which are otherwise difficult to characterize. This review summarizes various approaches used for analysis of the phosphoproteome in general, and protein kinases in particular, highlighting key cancer phosphoproteomic studies.

KW - Phosphorylation

KW - Protein microarrays

KW - Signal transduction

KW - SILAC

UR - http://www.scopus.com/inward/record.url?scp=78349310118&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78349310118&partnerID=8YFLogxK

U2 - 10.1016/j.molonc.2010.09.004

DO - 10.1016/j.molonc.2010.09.004

M3 - Review article

C2 - 20937571

AN - SCOPUS:78349310118

VL - 4

SP - 482

EP - 495

JO - Molecular Oncology

JF - Molecular Oncology

SN - 1574-7891

IS - 6

ER -